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| pubmed-article:9036855 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:9036855 | lifeskim:mentions | umls-concept:C1704332 | lld:lifeskim |
| pubmed-article:9036855 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
| pubmed-article:9036855 | lifeskim:mentions | umls-concept:C0060648 | lld:lifeskim |
| pubmed-article:9036855 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:9036855 | lifeskim:mentions | umls-concept:C0066697 | lld:lifeskim |
| pubmed-article:9036855 | pubmed:issue | 5304 | lld:pubmed |
| pubmed-article:9036855 | pubmed:dateCreated | 1997-3-18 | lld:pubmed |
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| pubmed-article:9036855 | pubmed:abstractText | Formate dehydrogenase H from Escherichia coli contains selenocysteine (SeCys), molybdenum, two molybdopterin guanine dinucleotide (MGD) cofactors, and an Fe4S4 cluster at the active site and catalyzes the two-electron oxidation of formate to carbon dioxide. The crystal structures of the oxidized [Mo(VI), Fe4S4(ox)] form of formate dehydrogenase H (with and without bound inhibitor) and the reduced [Mo(IV), Fe4S4(red)] form have been determined, revealing a four-domain alphabeta structure with the molybdenum directly coordinated to selenium and both MGD cofactors. These structures suggest a reaction mechanism that directly involves SeCys140 and His141 in proton abstraction and the molybdenum, molybdopterin, Lys44, and the Fe4S4 cluster in electron transfer. | lld:pubmed |
| pubmed-article:9036855 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9036855 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9036855 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9036855 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:9036855 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:9036855 | pubmed:author | pubmed-author:KhangulovS... | lld:pubmed |
| pubmed-article:9036855 | pubmed:author | pubmed-author:StadtmanT CTC | lld:pubmed |
| pubmed-article:9036855 | pubmed:author | pubmed-author:RohR ARA | lld:pubmed |
| pubmed-article:9036855 | pubmed:author | pubmed-author:BoyingtonJ... | lld:pubmed |
| pubmed-article:9036855 | pubmed:author | pubmed-author:GladyshevV... | lld:pubmed |
| pubmed-article:9036855 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9036855 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:9036855 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:9036855 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9036855 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9036855 | pubmed:pagination | 1305-8 | lld:pubmed |
| pubmed-article:9036855 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:9036855 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9036855 | pubmed:articleTitle | Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster. | lld:pubmed |
| pubmed-article:9036855 | pubmed:affiliation | Laboratory of Molecular Structure, National Institute of Allergy and Infectious Diseases, National Institutes of Health (NIH), Rockville, MD 20852, USA. | lld:pubmed |
| pubmed-article:9036855 | pubmed:publicationType | Journal Article | lld:pubmed |
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